1e89 - Revision history

OCA at 11:56, 13 December 2023

2023-12-13T11:56:04Z

←Older revision		Revision as of 11:56, 13 December 2023
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	<StructureSection load='1e89' size='340' side='right'caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1e89' size='340' side='right'caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Cassava Cassava~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E89 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E89 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1dwo\|1dwo]]~~, [[~~1dwp~~\|~~1dwp~~]]~~, [[1dwq\|1dwq]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.1Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.~~4 3.3.2.4] </span>~~</td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [https://pdbe.org/1e89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [https://www.ebi.ac.uk/pdbsum/1e89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e89 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [https://pdbe.org/1e89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [https://www.ebi.ac.uk/pdbsum/1e89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e89 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/HNL_MANES HNL_MANES] Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Cassava]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Trans-epoxysuccinate hydrolase~~]]	+	[[Category: Manihot esculenta]]
-	[[Category: Effenberger, F]]	+	[[Category: Effenberger F]]
-	[[Category: Foerster, S]]	+	[[Category: Foerster S]]
-	[[Category: Lauble, H]]	+	[[Category: Lauble H]]
-	[[Category: Miehlich, B]]	+	[[Category: Miehlich B]]
-	[[Category: Wajant, H]]	+	[[Category: Wajant H]]
-	~~[[Category: Acetone cyanohydrin complex]]~~	+
-	~~[[Category: Active site mutant]]~~	+
-	~~[[Category: Hydroxynitrile lyase]]~~	+
-	~~[[Category: Lyase~~]]	+

OCA at 05:45, 28 April 2021

2021-04-28T05:45:52Z

←Older revision		Revision as of 05:45, 28 April 2021
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	<StructureSection load='1e89' size='340' side='right'caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1e89' size='340' side='right'caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Cassava Cassava]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1E89 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cassava Cassava]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E89 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [~~http~~://pdbe.org/1e89 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1e89 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1e89 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [https://pdbe.org/1e89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [https://www.ebi.ac.uk/pdbsum/1e89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e89 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 06:36, 24 July 2019

2019-07-24T06:36:39Z

←Older revision		Revision as of 06:36, 24 July 2019
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	==ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN==		==ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN==
-	<StructureSection load='1e89' size='340' side='right' caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1e89' size='340' side='right'caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cassava Cassava]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cassava Cassava]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Cassava]]		[[Category: Cassava]]
		+	[[Category: Large Structures]]
	[[Category: Trans-epoxysuccinate hydrolase]]		[[Category: Trans-epoxysuccinate hydrolase]]
	[[Category: Effenberger, F]]		[[Category: Effenberger, F]]

OCA at 08:02, 13 December 2017

2017-12-13T08:02:37Z

←Older revision		Revision as of 08:02, 13 December 2017
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		+
	==ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN==		==ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN==
	<StructureSection load='1e89' size='340' side='right' caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1e89' size='340' side='right' caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://pdbe.org/1e89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://pdbe.org/1e89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e89 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/1e89_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/1e89_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 04:22, 9 February 2016

2016-02-09T04:22:53Z

←Older revision		Revision as of 04:22, 9 February 2016
Line 15:		Line 15:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e89 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 18:35, 10 September 2015

2015-09-10T18:35:46Z

←Older revision		Revision as of 18:35, 10 September 2015
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	<StructureSection load='1e89' size='340' side='right' caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1e89' size='340' side='right' caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Manihot_esculenta Manihot esculenta~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cassava Cassava]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://pdbe.org/1e89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1e89" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Manihot esculenta~~]]	+	[[Category: Cassava]]
	[[Category: Trans-epoxysuccinate hydrolase]]		[[Category: Trans-epoxysuccinate hydrolase]]
	[[Category: Effenberger, F]]		[[Category: Effenberger, F]]

OCA at 21:12, 22 December 2014

2014-12-22T21:12:38Z

←Older revision		Revision as of 21:12, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Manihot esculenta]]		[[Category: Manihot esculenta]]
	[[Category: Trans-epoxysuccinate hydrolase]]		[[Category: Trans-epoxysuccinate hydrolase]]
-	[[Category: Effenberger, F.]]	+	[[Category: Effenberger, F]]
-	[[Category: Foerster, S.]]	+	[[Category: Foerster, S]]
-	[[Category: Lauble, H.]]	+	[[Category: Lauble, H]]
-	[[Category: Miehlich, B.]]	+	[[Category: Miehlich, B]]
-	[[Category: Wajant, H.]]	+	[[Category: Wajant, H]]
	[[Category: Acetone cyanohydrin complex]]		[[Category: Acetone cyanohydrin complex]]
	[[Category: Active site mutant]]		[[Category: Active site mutant]]
	[[Category: Hydroxynitrile lyase]]		[[Category: Hydroxynitrile lyase]]
	[[Category: Lyase]]		[[Category: Lyase]]

OCA at 15:30, 29 September 2014

2014-09-29T15:30:50Z

←Older revision		Revision as of 15:30, 29 September 2014
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-	[[~~Image:~~1e89.~~png~~\|~~left~~\|200px]]	+	==ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN==
		+	<StructureSection load='1e89' size='340' side='right' caption='[[1e89]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dwo\|1dwo]], [[1dwp\|1dwp]], [[1dwq\|1dwq]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/1e89_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The structure and function of hydroxynitrile lyase from Manihot esculenta (MeHNL) have been analyzed by X-ray crystallography and site-directed mutagenesis. The crystal structure of the MeHNL-S80A mutant enzyme has been refined to an R-factor of 18.0% against diffraction data to 2.1-A resolution. The three-dimensional structure of the MeHNL-S80A-acetone cyanohydrin complex was determined at 2.2-A resolution and refined to an R-factor of 18.7%. Thr11 and Cys81 involved in substrate binding have been substituted by Ala in site-directed mutagenesis. The kinetic measurements of these mutant enzymes are presented. Combined with structural data, the results support a mechanism for cyanogenesis in which His236 as a general base abstracts a proton from Ser80, thereby allowing proton transfer from the hydroxyl group of acetone cyanohydrin to Ser80. The His236 imidazolium cation then facilitates the leaving of the nitrile group by proton donating.

-	~~{{STRUCTURE_1e89\| PDB=1e89 \| SCENE= }}~~	+	Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin.,Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F Protein Sci. 2001 May;10(5):1015-22. PMID:11316882<ref>PMID:11316882</ref>

-	~~===ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11316882}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1e89]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Manihot_esculenta Manihot esculenta]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:011316882<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Manihot esculenta]]		[[Category: Manihot esculenta]]
	[[Category: Trans-epoxysuccinate hydrolase]]		[[Category: Trans-epoxysuccinate hydrolase]]

OCA at 09:48, 16 January 2013

2013-01-16T09:48:29Z

←Older revision		Revision as of 09:48, 16 January 2013
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	[[Image:1e89.png\|left\|200px]]		[[Image:1e89.png\|left\|200px]]

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	===ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN===		===ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN===

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	{{ABSTRACT_PUBMED_11316882}}		{{ABSTRACT_PUBMED_11316882}}

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	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11316882</ref><ref group="xtra">PMID:11173464~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011316882</ref><references group="xtra"/>
	[[Category: Manihot esculenta]]		[[Category: Manihot esculenta]]
	[[Category: Trans-epoxysuccinate hydrolase]]		[[Category: Trans-epoxysuccinate hydrolase]]

OCA: Protected "1e89" [edit=sysop:move=sysop]

2011-03-14T23:40:13Z

Protected "1e89" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:40, 14 March 2011